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Papers
61,005 resultsShowing papers similar to Whether the wobbling W156 is a pre-requisite for efficient PET biodegradation by IsPETase
ClearMarine PET Hydrolase (PET2): Assessment of Terephthalate- and Indole-Based Polyesters Depolymerization
Researchers characterized a marine enzyme (PET2) capable of breaking down PET plastic and related polyester materials under relatively mild conditions. Discovering and engineering enzymes that can degrade PET could help address the massive accumulation of PET microplastics in ocean environments.
Discovery and rational engineering of PET hydrolase with both mesophilic and thermophilic PET hydrolase properties
Researchers discovered a new enzyme from a soil bacterium that can break down PET plastic — the material in most plastic bottles — at both room temperature and elevated heat, then engineered an improved version that degrades PET powder almost completely within half a day at 55°C. This dual-temperature capability makes it more practical than existing enzymes for industrial-scale plastic recycling and could help address the global PET waste problem.
An Overview into Polyethylene Terephthalate (PET) Hydrolases and Efforts in Tailoring Enzymes for Improved Plastic Degradation
This review examines the discovery and engineering of PET-degrading enzymes including PETase and cutinase variants, discussing protein engineering strategies to improve catalytic efficiency and thermostability for practical biodegradation of polyethylene terephthalate plastic waste.
Recent advances in enzyme engineering for improved deconstruction of poly(ethylene terephthalate) (PET) plastics
This review covers recent progress in engineering enzymes that can break down PET plastic, the material used in water bottles and food containers. While natural enzymes that digest PET have been discovered, they are not yet fast or durable enough for industrial-scale recycling. Advances in protein engineering, directed evolution, and computational design are steadily improving these enzymes, which could eventually provide a sustainable way to recycle PET and reduce microplastic pollution at its source.
Perspectives on the Role of Enzymatic Biocatalysis for the Degradation of Plastic PET
This review discusses the role of enzymatic biocatalysis in PET plastic degradation, examining how the discovery of PETase and subsequent enzyme engineering have advanced biodegradation as an alternative to chemical and mechanical recycling for one of the most produced plastics globally.
Biodegradation of highly crystallized poly(ethylene terephthalate) through cell surface codisplay of bacterial PETase and hydrophobin
Researchers engineered yeast cells to display both a PET-degrading enzyme (PETase) and a sticky protein (hydrophobin) on their surface simultaneously, dramatically improving the breakdown of highly crystalline PET plastic — achieving a 329-fold increase in degradation rate compared to the purified enzyme alone. This whole-cell biocatalyst approach could make enzymatic plastic recycling far more practical and efficient.
A versatile assay platform for enzymatic poly(ethylene-terephthalate) degradation
Researchers developed a fast, reliable assay platform for testing enzymes that break down PET plastic, a common component of bottles and packaging. Better enzyme-based recycling tools could help reduce PET accumulation in the environment and the microplastics it generates.
Enhancing PET Degrading Enzymes: A Combinatory Approach
Scientists worked on improving enzymes that can break down PET plastic, one of the most common plastics in consumer products. Using a combinatory approach, researchers enhanced the performance of a naturally occurring PET-degrading enzyme from the bacterium Piscinibacter sakaiensis. The study suggests that engineered enzymes could eventually help create a circular economy for plastic waste by enabling efficient recycling at the molecular level.
Enzymatic Degradation of PET plastic
This study tested commercial-grade enzymes for degrading PET plastic and found that enzymatic degradation was effective at laboratory scale but faced challenges for real-world application. Scaling up enzymatic PET recycling could reduce the persistence of plastic waste that eventually fragments into microplastics in the environment.
Enhanced degradation of polyethylene terephthalate (PET) microplastics by an engineered Stenotrophomonas pavanii in the presence of biofilm
Scientists engineered a biofilm-forming bacterium to break down PET microplastics (the type found in water bottles and food containers) at room temperature. The engineered bacteria achieved significant PET degradation over 30 days and also worked on other polyester plastics, offering a potential biological solution for cleaning up microplastic pollution in water environments.
Enzymatic Remediation of Polyethylene Terephthalate (PET)–Based Polymers for Effective Management of Plastic Wastes: An Overview
Enzymatic approaches for remediating PET-based plastic waste were reviewed, covering PETase and related enzymes that can break PET into reusable monomers. Enzyme engineering strategies to improve thermostability and catalytic efficiency are discussed as a pathway to scalable biological PET recycling.
Eco-Microbiology: Discovering Biochemical Enhancers of PET Biodegradation by Piscinibacter sakaiensis
This paper reviews biochemical strategies for enhancing PET biodegradation by microorganisms, focusing on the discovery and engineering of plastic-degrading enzymes. The review highlights recent advances and remaining challenges in scaling up enzymatic plastic degradation for industrial applications.
Marine PET Hydrolase (PET2): Assessment of Terephthalate- and Indole-Based Polyester Depolymerization
This study characterized a marine-derived enzyme (PET2) capable of breaking down PET plastic under mild conditions, assessing its efficiency for enzymatic recycling. Enzyme-based PET recycling could prevent plastic waste from fragmenting into the microplastics that accumulate in oceans and organisms.
Targeted aggregation of PETase towards surface of Stenotrophomonas pavanii for degradation of PET microplastics
Researchers developed a strategy to target PETase enzyme to the surface of Stenotrophomonas pavanii bacteria, improving the efficiency of in-situ PET microplastic degradation. Surface-displayed PETase showed significantly enhanced PET hydrolysis compared to free enzyme, offering a practical approach to microbial degradation of dispersed PET microplastics in environmental settings.
Current Knowledge on Polyethylene Terephthalate Degradation by Genetically Modified Microorganisms
This review covers genetically modified microorganisms engineered to degrade polyethylene terephthalate, examining how bioengineering of enzymes such as PETase and enhanced expression systems can overcome the low biodegradation rates of wild-type microorganisms toward this ubiquitous plastic.
Computational Redesign of a PETase for Plastic Biodegradation under Ambient Condition by the GRAPE Strategy
Researchers developed a computational protein engineering strategy called GRAPE to redesign a PET-degrading enzyme from Ideonella sakaiensis. The resulting DuraPETase variant showed a 31-degree-Celsius increase in thermal stability and over 300-fold improved degradation of PET films at mild temperatures, achieving complete biodegradation of 2 g/L microplastics into water-soluble products under ambient conditions.
Computational redesign of a PETase for plastic biodegradation by the GRAPE strategy
Researchers engineered a more stable version of the enzyme PETase, which breaks down PET plastic, using a computational protein design strategy. The improved enzyme could enable more efficient industrial biodegradation of PET plastic waste, including microplastics.
Application of PETase in Plastic Biodegradation and Its Synthesis
This review examines how PETase enzymes can be used to biodegrade plastic waste, particularly polyethylene terephthalate, which is one of the most widely used plastics globally. Researchers discuss recent advances in modifying PETase enzymes for improved efficiency and establishing sustainable synthesis platforms. The study suggests that enzymatic biodegradation offers a promising biological solution to the growing plastic pollution crisis.
Enzymatic PET Degradation
This review examines enzymatic degradation of PET (polyethylene terephthalate), the plastic used in bottles and polyester clothing, as a promising pathway for breaking down this persistent polymer. Advances in engineering more efficient PET-degrading enzymes could enable industrial-scale biological recycling and reduce the environmental accumulation of PET microplastics.
Enzymatic Degradation of Polyethylene Terephthalate Plastics by Bacterial Curli Display PETase
Researchers engineered bacteria to display a PET-degrading enzyme on their surface, creating a reusable biocatalyst capable of breaking down polyethylene terephthalate plastics. The system worked under various conditions, remained stable for at least 30 days, and could even degrade PET microplastics in wastewater and highly crystalline consumer plastic waste. This biological approach offers a promising environmentally friendly alternative for plastic recycling and waste treatment.
An efficient strategy to tailor PET hydrolase: Simple preparation with high yield and enhanced hydrolysis to micro-nano plastics
This study developed a simplified, high-yield preparation method for PET-degrading hydrolase enzymes to improve their ability to break down PET nano- and microplastics. The engineered enzyme showed enhanced hydrolysis activity against PET microplastics, offering a more practical route to enzymatic plastic waste treatment.
Explorations of Polyethylene Terephthalate (PET) Hydrolase for addressing PET Plastic Pollution
This review explores the biology of PETase enzymes and their potential for addressing PET plastic pollution, covering the discovery of Ideonella sakaiensis and subsequent enzyme engineering efforts. Developing efficient PET-degrading enzymes is a promising biotechnological strategy for reducing plastic pollution at scale.
On the Role of Temperature in the Depolymerization of PET by FAST‐PETase: An Atomistic Point of View on Possible Active Site Pre‐Organization and Substrate‐Destabilization Effects
Researchers used molecular simulations to understand why the plastic-degrading enzyme FAST-PETase works better at 50°C than at lower temperatures when breaking down PET plastic. They found that at the optimal temperature the enzyme's active site pre-organizes itself to bind PET more efficiently, and the enzyme forces the plastic into a more reactive shape. Understanding these mechanisms can guide the engineering of even more effective enzymes for breaking down PET microplastics and plastic waste at practical scales.
Directed Immobilization of PETase on Mesoporous Silica Enables Sustained Depolymerase Activity in Synthetic Wastewater Conditions
Researchers developed a PETase enzyme immobilized on mesoporous silica nanoparticles that showed up to 6.2-fold increased activity and 2.5-fold enhanced stability for degrading PET microfibers under simulated wastewater conditions.